Differentiation of Tyrosine Hydroxylase and Phenol Oxidase after Electrophoresis

Nellaiappan, K.; Valivittan, K.

doi:10.3109/10520299309105630

Cited by 4 publications

(1 citation statement)

References 3 publications

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“…Insect prophenoloxidase (PPO) is also an important innate immune protein as it is involved in cellular and humoral defenses [69] . Tyrosine hydroxylase can convert tyrosine to o-diphenols, whereas phenoloxidase can convert o-diphenols to quinones [70] . The phenoloxidases of perennial plants have hydroxylase activity [71] .…”

Section: Introductionmentioning

confidence: 99%

COVID-19: Attacks the 1-Beta Chain of Hemoglobin to Disrupt Respiratory Function and Escape Immunity by Capsid-Like System

Liu

2023

Preprint

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The genetic recombination of the SARs-CoV-2 virus in bats may result in behaviors comparable to those of certain RNA viruses. This cross-activity helps explain SARs-CoV-2's strange respiratory symptoms and immune evasion abilities. In this present study, the biological roles of SARs-CoV-2 proteins were investigated utilizing bioinformatic techniques involving the search for conserved domains. According to the study, the S and ORF3a proteins of SARs-CoV-2 possess picornavirus/calicivirus capsid domains, can bind hemoglobin, heme, and porphyrin. Both Arg134 of ORF3a and Cys44 of E are iron-binding sites for heme. The ORF3a protein has a region that converts heme into iron and porphyrin. In addition to chitin and polyphenol binding domains, the S protein also contains hemocyanin and phenoloxidase-like domains. The S protein constructs Fe-polyphenol complexes to link the red blood cell membrane, allowing SARs-CoV-2 to hitch a ride on red blood cells for fast delivery to target organs. This type of capsid-like vector delays the immune system but does not significantly alter the function of red blood cells to transport oxygen. Due to the distortion of the cell membrane, red blood cells with an excess of viral particles release hemoglobin to harm the virus. The wbl domains of the S protein respond to nitration, and then phenoloxidase domains oxidize polyphenols, allowing the virus to shed from the red blood cell membrane. ORF3a also attack 1-beta chain of hemoglobin; however, the majority of hemoglobin may retain its native structure. Patients will have variable degrees of respiratory distress and coagulation symptoms, but the hemocyanin domains of the S protein can improve a patient's respiratory status by transporting oxygen.

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Section: Introductionmentioning

confidence: 99%

COVID-19: Attacks the 1-Beta Chain of Hemoglobin to Disrupt Respiratory Function and Escape Immunity by Capsid-Like System

Liu

2023

Preprint

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Oxidative metabolism of dopamine: A colour reaction from human midbrain analysed by mass spectrometry

Iuliis

Arrigoni

Andersson

et al. 2008

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Electrophoretic Separation and Identification of Phenoloxidases in Hemolymph and Midgut of Adult Anopheles stephensi Mosquitoes

Sidjanski

Mathews²,

Vanderberg³

1997

The Journal of Parasitology

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Anopheles mosquitoes frequently respond to invading malaria parasites with a rejection mechanism consisting of phenoloxidase-mediated melanization of ookinetes in the mosquito midgut epithelium. The relative roles of hemolymph vs. midgut phenoloxidase in this rejection mechanism is unclear. We have separated and identified phenoloxidase isozymes from midgut and hemolymph of Anopheles stephensi by native gel electrophoresis followed by zymography. The isozymes from the 2 sites had distinctively different electrophoretic characteristics. Hemolymph possessed 2 phenoloxidase-positive bands, both of which were bifunctional molecules that oxidized monophenol as well as o-diphenol substrates. Midgut extract possessed 3 bands that migrated more rapidly than those of the hemolymph. None of these midgut bands had detectable monophenoloxidase activity; they possessed, however, a broad spectrum of diphenoloxidase activity in their ability to oxidize both o- and p-diphenol substrates, as well as the laccase substrate syringaldazine. The 2 most rapidly migrating midgut PO bands could be distinguished from the more slowly migrating band through their insensitivity to inhibition by the chelating agent tropolone. A question to be resolved in the future relates to the relative roles of hemolymph vs. midgut phenoloxidase in mosquito defense against invasive parasites.

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Differentiation of Tyrosine Hydroxylase and Phenol Oxidase after Electrophoresis

Cited by 4 publications

References 3 publications

COVID-19: Attacks the 1-Beta Chain of Hemoglobin to Disrupt Respiratory Function and Escape Immunity by Capsid-Like System

COVID-19: Attacks the 1-Beta Chain of Hemoglobin to Disrupt Respiratory Function and Escape Immunity by Capsid-Like System

Oxidative metabolism of dopamine: A colour reaction from human midbrain analysed by mass spectrometry

Electrophoretic Separation and Identification of Phenoloxidases in Hemolymph and Midgut of Adult Anopheles stephensi Mosquitoes

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